P. Tompa, Intrinsically unstructured proteins, Trends in Biochemical Sciences, vol.27, issue.10, pp.527-533, 2002.
DOI : 10.1016/S0968-0004(02)02169-2

V. N. Uversky, A. K. Dunker, I. Silman, V. N. Uversky, J. L. Sussman et al., Natively unfolded proteins: a point where biology waits for physics Function and structure of inherently disordered proteins, Protein Sci. Curr. Opin. Struct. Biol. Nat. Rev. Mol. Cell Biol, vol.11, issue.6, pp.739-756, 2002.

H. J. Dyson, Expanding the proteome: disordered and alternatively folded proteins, Quarterly Reviews of Biophysics, vol.78, issue.04, pp.1-52, 2011.
DOI : 10.1016/j.bbrc.2009.02.151

A. Huang and C. M. Stultz, Finding order within disorder: elucidating the structure of proteins associated with neurodegenerative disease, Future Medicinal Chemistry, vol.1, issue.3, pp.467-482, 2009.
DOI : 10.4155/fmc.09.40

V. N. Uversky, Intrinsic disorder in proteins associated with neurodegenerative diseases, Frontiers in Bioscience, vol.14, issue.1, pp.5188-5238, 2009.
DOI : 10.2741/3594

A. L. Fink, Natively unfolded proteins, Current Opinion in Structural Biology, vol.15, issue.1, pp.35-41, 2005.
DOI : 10.1016/j.sbi.2005.01.002

J. Wang, Z. Cao, L. Zhao, L. , and S. , Novel Strategies for Drug Discovery Based on Intrinsically Disordered Proteins (IDPs), International Journal of Molecular Sciences, vol.12, issue.12, pp.3205-3219, 2011.
DOI : 10.3390/ijms12053205

Y. Cheng, T. Legall, C. J. Oldfield, J. P. Mueller, Y. J. Van et al., Rational drug design via intrinsically disordered protein, Trends in Biotechnology, vol.24, issue.10, pp.435-442, 2006.
DOI : 10.1016/j.tibtech.2006.07.005

V. N. Uversky, Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes, Chem. Soc. Rev., vol.1, issue.suppl 1, pp.1623-1634, 2011.
DOI : 10.1039/C0CS00057D

K. Sugase, H. J. Dyson, W. , and P. E. , Mechanism of coupled folding and binding of an intrinsically disordered protein, Nature, vol.42, issue.7147, pp.1021-1025, 2007.
DOI : 10.1038/nature05858

A. P. Demchenko, Recognition between flexible protein molecules: induced and assisted folding, Journal of Molecular Recognition, vol.6, issue.1, pp.42-61, 2001.
DOI : 10.1002/1099-1352(200101/02)14:1<42::AID-JMR518>3.0.CO;2-8

H. J. Dyson, W. , and P. E. , Coupling of folding and binding for unstructured proteins, Current Opinion in Structural Biology, vol.12, issue.1, pp.54-60, 2002.
DOI : 10.1016/S0959-440X(02)00289-0

C. J. Oldfield, J. Meng, J. Y. Yang, M. Q. Yang, V. N. Uversky et al., Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners, BMC Genomics, vol.9, issue.Suppl 1, p.1, 2008.
DOI : 10.1186/1471-2164-9-S1-S1

P. Tompa and M. Fuxreiter, Fuzzy complexes: polymorphism and structural disorder in protein???protein interactions, Trends in Biochemical Sciences, vol.33, issue.1, pp.2-8, 2008.
DOI : 10.1016/j.tibs.2007.10.003

C. K. Fisher and C. M. Stultz, Constructing ensembles for intrinsically disordered proteins, Current Opinion in Structural Biology, vol.21, issue.3, pp.426-431, 2011.
DOI : 10.1016/j.sbi.2011.04.001

D. Eliezer, Characterizing Residual Structure in Disordered Protein States Using Nuclear Magnetic Resonance, Methods Mol. Biol, vol.350, pp.49-67, 2007.
DOI : 10.1385/1-59745-189-4:49

H. J. Dyson, W. , and P. E. , Equilibrium NMR studies of unfolded and partially folded proteins, Nature Structural Biology, vol.91, issue.7, pp.499-503, 1998.
DOI : 10.1006/jmbi.1997.1369

H. J. Dyson, W. , and P. E. , Unfolded Proteins and Protein Folding Studied by NMR, Chemical Reviews, vol.104, issue.8, pp.3607-3622, 2004.
DOI : 10.1021/cr030403s

M. R. Hansen, L. Mueller, and A. Pardi, Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions, Nature Structural Biology, vol.85, issue.12, pp.1065-1074, 1998.
DOI : 10.1021/ja953186o

G. M. Clore, M. R. Starich, and A. M. Gronenborn, Measurement of Residual Dipolar Couplings of Macromolecules Aligned in the Nematic Phase of a Colloidal Suspension of Rod-Shaped Viruses, Journal of the American Chemical Society, vol.120, issue.40, pp.10571-10572, 1998.
DOI : 10.1021/ja982592f

J. Torbet, G. Maret, H. J. Sass, G. Musco, S. J. Stahl et al., Fibres of highly oriented Pf1 bacteriophage produced in a strong magnetic field Solution NMR of proteins within polyacrylamide gels: diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes, J. Mol. Biol. J. Biomol. NMR, vol.134, issue.18, pp.843-845, 1979.

R. Tycko, F. J. Blanco, and Y. Ishii, Alignment of Biopolymers in Strained Gels:?? A New Way To Create Detectable Dipole???Dipole Couplings in High-Resolution Biomolecular NMR, Journal of the American Chemical Society, vol.122, issue.38, pp.9340-9341, 2000.
DOI : 10.1021/ja002133q

M. Rückert and G. Otting, Alignment of Biological Macromolecules in Novel Nonionic Liquid Crystalline Media for NMR Experiments, Journal of the American Chemical Society, vol.122, issue.32, pp.7793-7797, 2000.
DOI : 10.1021/ja001068h

J. R. Tolman, J. M. Flanagan, M. A. Kennedy, and J. H. Prestegard, Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution., Proceedings of the National Academy of Sciences, vol.92, issue.20, pp.9279-9283, 1995.
DOI : 10.1073/pnas.92.20.9279

R. W. Woody, Circular Dichroism Spectrum of Peptides in the Poly(Pro)II Conformation, Journal of the American Chemical Society, vol.131, issue.23, pp.8234-8245, 2009.
DOI : 10.1021/ja901218m

M. Kjaergaard, S. Brander, F. M. Poulsen, E. Eyal, R. Najmanovich et al., Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH, Journal of Biomolecular NMR, vol.25, issue.2, pp.139-149, 2004.
DOI : 10.1007/s10858-011-9472-x

R. L. Kingston, W. A. Baase, and L. S. Gay, Characterization of Nucleocapsid Binding by the Measles Virus and Mumps Virus Phosphoproteins, Journal of Virology, vol.78, issue.16, pp.8630-8640, 2004.
DOI : 10.1128/JVI.78.16.8630-8640.2004

J. Curran, J. B. Marq, and D. Kolakofsky, An N-­?terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication, J. Virol, vol.69, pp.849-855, 1995.

M. Mavrakis, S. Méhouas, E. Réal, F. Iseni, D. Blondel et al., Rabies virus chaperone: Identification of the phosphoprotein peptide that keeps nucleoprotein soluble and free from non-specific RNA, Virology, vol.349, issue.2, pp.422-429, 2006.
DOI : 10.1016/j.virol.2006.01.030

M. Chen, T. Ogino, and A. K. Banerjee, Interaction of Vesicular Stomatitis Virus P and N Proteins: Identification of Two Overlapping Domains at the N Terminus of P That Are Involved in N0-P Complex Formation and Encapsidation of Viral Genome RNA, Journal of Virology, vol.81, issue.24, pp.13478-13485, 2007.
DOI : 10.1128/JVI.01244-07

D. Karlin, F. Ferron, B. Canard, and S. Longhi, Structural disorder and modular organization in Paramyxovirinae N and P, Journal of General Virology, vol.84, issue.12, pp.3239-3252, 2003.
DOI : 10.1099/vir.0.19451-0

K. Johansson, J. Bourhis, V. Campanacci, C. Cambillau, B. Canard et al., Crystal Structure of the Measles Virus Phosphoprotein Domain Responsible for the Induced Folding of the C-terminal Domain of the Nucleoprotein, Journal of Biological Chemistry, vol.278, issue.45, pp.44567-44573, 2003.
DOI : 10.1074/jbc.M308745200

N. Tarbouriech, J. Curran, R. W. Ruigrok, and W. P. Burmeister, Tetrameric coiled coil domain of Sendai virus phosphoprotein, Nat. Struct. Biol, vol.7, pp.777-781, 2000.

L. Blanchard, N. Tarbouriech, M. Blackledge, P. Timmins, W. P. Burmeister et al., Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution, Virology, vol.319, issue.2, pp.201-211, 2004.
DOI : 10.1016/j.virol.2003.10.029

G. Schoehn, M. Mavrakis, A. Albertini, R. Wade, A. Hoenger et al., The 12?? Structure of Trypsin-treated Measles Virus N???RNA, Journal of Molecular Biology, vol.339, issue.2, pp.301-312, 2004.
DOI : 10.1016/j.jmb.2004.03.073

D. Bhella, A. Ralph, and R. P. Yeo, Conformational Flexibility in Recombinant Measles Virus Nucleocapsids Visualised by Cryo-negative Stain Electron Microscopy and Real-space Helical Reconstruction, Journal of Molecular Biology, vol.340, issue.2, pp.319-331, 2004.
DOI : 10.1016/j.jmb.2004.05.015

A. Desfosses, G. Goret, L. Farias-estrozi, R. W. Ruigrok, and I. Gutsche, Nucleoprotein-RNA Orientation in the Measles Virus Nucleocapsid by Three-Dimensional Electron Microscopy, Journal of Virology, vol.85, issue.3, pp.1391-1395, 2011.
DOI : 10.1128/JVI.01459-10

R. G. Tawar, S. Duquerroy, C. Vonrhein, P. F. Varela, L. Damier-­?piolle et al., Crystal Structure of a Nucleocapsid-Like Nucleoprotein-RNA Complex of Respiratory Syncytial Virus, Structure of a Nucleocapsid-­?Like Nucleoprotein-­?RNA Complex of Respiratory Syncytial Virus, pp.1279-1283, 2009.
DOI : 10.1126/science.1177634
URL : https://hal.archives-ouvertes.fr/pasteur-00457523

G. Porod, In small angle x-­?ray scattering, 1982.

J. J. Skalicky, J. L. Mills, S. Sharma, and T. Szyperski, Aromatic Ring-Flipping in Supercooled Water:?? Implications for NMR-Based Structural Biology of Proteins, Journal of the American Chemical Society, vol.123, issue.3, 2001.
DOI : 10.1021/ja003220l

J. L. Mills and T. Szyperski, Protein dynamics in supercooled water: the search for slow motional modes, Journal of Biomolecular NMR, vol.23, issue.1, pp.63-67, 2002.
DOI : 10.1023/A:1015397305148

T. Szyperski and J. L. Mills, NMR-based structural biology of proteins in supercooled water, Journal of Structural and Functional Genomics, vol.132, issue.1, pp.1-7, 2011.
DOI : 10.1007/s10969-011-9111-5

G. Otting, Protein NMR Using Paramagnetic Ions, Annual Review of Biophysics, vol.39, issue.1, pp.387-405, 2010.
DOI : 10.1146/annurev.biophys.093008.131321

R. J. Kurland and B. R. Mcgarvey, Isotropic NMR shifts in transition metal complexes: The calculation of the fermi contact and pseudocontact terms, Journal of Magnetic Resonance (1969), vol.2, issue.3, pp.286-301, 1970.
DOI : 10.1016/0022-2364(70)90100-9

M. Allegrozzi, I. Bertini, M. B. Janik, Y. Lee, G. Liu et al., Lanthanide-Induced Pseudocontact Shifts for Solution Structure Refinements of Macromolecules in Shells up to 40 ?? from the Metal Ion, Journal of the American Chemical Society, vol.122, issue.17, pp.4154-4161, 2000.
DOI : 10.1021/ja993691b

F. Rodriguez-­?castañeda, P. Haberz, A. Leonov, and C. Griesinger, Paramagnetic tagging of diamagnetic proteins for solution NMR, Magnetic Resonance in Chemistry, vol.46, issue.S1, pp.10-16, 2006.
DOI : 10.1002/mrc.1811

L. Chang, K. , and M. , Mammalian MAP kinase signalling cascades, Nature, vol.410, issue.6824, pp.37-40, 2001.
DOI : 10.1038/35065000

N. J. Kennedy, H. K. Sluss, S. N. Jones, D. Bar-­?sagi, R. A. Flavell et al., Suppression of Ras-stimulated transformation by the JNK signal transduction pathway, Genes & Development, vol.17, issue.5, pp.629-637, 2003.
DOI : 10.1101/gad.1062903

J. Hirosumi, G. Tuncman, L. Chang, C. Z. Görgün, K. T. Uysal et al., A central role for JNK in obesity and insulin resistance, Nature, vol.141, issue.6913, pp.333-336, 2002.
DOI : 10.1073/pnas.251194298

H. Yoshida, C. J. Hastie, H. Mclauchlan, P. Cohen, and M. Goedert, Phosphorylation of microtubule-associated protein tau by isoforms of c-Jun N-terminal kinase (JNK), Journal of Neurochemistry, vol.90, issue.2, pp.352-358, 2004.
DOI : 10.1111/j.1471-4159.2004.02479.x

X. G. Xia, T. Harding, M. Weller, A. Bieneman, J. B. Uney et al., Gene transfer of the JNK interacting protein-1 protects dopaminergic neurons in the MPTP model of Parkinson's disease, Proceedings of the National Academy of Sciences, vol.98, issue.18, pp.10433-10438, 2001.
DOI : 10.1073/pnas.181182298

L. Bardwell, Mechanisms of MAPK signalling specificity, Biochemical Society Transactions, vol.34, issue.5, pp.837-841, 2006.
DOI : 10.1042/BST0340837

A. J. Bardwell, E. Frankson, and L. Bardwell, Selectivity of Docking Sites in MAPK Kinases, Journal of Biological Chemistry, vol.284, issue.19, pp.13165-13173, 2009.
DOI : 10.1074/jbc.M900080200

C. R. Weston, D. G. Lambright, D. , and R. J. , SIGNAL TRANSDUCTION: MAP Kinase Signaling Specificity, Science, vol.296, issue.5577, pp.2345-2347, 2002.
DOI : 10.1126/science.1073344

E. J. Goldsmith, R. Akella, X. Min, T. Zhou, and J. M. Humphreys, Substrate and Docking Interactions in Serine/Threonine Protein Kinases, Chemical Reviews, vol.107, issue.11, pp.5065-5081, 2007.
DOI : 10.1021/cr068221w

Z. Dosztányi, V. Csizmok, P. Tompa, and I. Simon, IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content, Bioinformatics, vol.21, issue.16, pp.3433-3434, 2005.
DOI : 10.1093/bioinformatics/bti541

A. D. Sharrocks, S. H. Yang, and A. Galanis, Docking domains and substrate-specificity determination for MAP kinases, Trends in Biochemical Sciences, vol.25, issue.9, pp.448-453, 2000.
DOI : 10.1016/S0968-0004(00)01627-3

M. Dickens, J. Rogers, J. Cavanagh, A. Raitano, Z. Xia et al., A Cytoplasmic Inhibitor of the JNK Signal Transduction Pathway, Science, vol.277, issue.5326, pp.693-696, 1997.
DOI : 10.1126/science.277.5326.693

C. Bonny, A. Oberson, S. Negri, C. Sauser, and D. Schorderet, Cell-Permeable Peptide Inhibitors of JNK: Novel Blockers of ??-Cell Death, Diabetes, vol.50, issue.1, pp.77-82, 2001.
DOI : 10.2337/diabetes.50.1.77

A. Whitmarsh, L. Cavanagh, C. Tournier, L. Yasuda, D. et al., A Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation, Science, vol.281, issue.5383, pp.1671-1674, 1998.
DOI : 10.1126/science.281.5383.1671

O. Kristensen, S. Guenat, I. Dar, N. Allaman-­?pillet, A. Abderrahmani et al., A unique set of SH3???SH3 interactions controls IB1 homodimerization, The EMBO Journal, vol.276, issue.4, pp.785-797, 2006.
DOI : 10.1038/sj.emboj.7600982

J. Yasuda, A. J. Whitmarsh, J. Cavanagh, M. Sharma, D. et al., The JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins, Molecular and Cellular Biology, vol.19, issue.10, pp.7245-7254, 1999.
DOI : 10.1128/MCB.19.10.7245

D. Young and N. Prize, Awarded to young researcher who has conducted particularly promising research within NMR spectroscopy. Grants and stipends 03 Grant from the French Agence National de la Recherche (ANR) (260.000 Euros) for the project Structural basis of molecular recognition in intrinsically disordered proteins " 01, Grant from the Lundbeck foundation, Denmark (59.900 Euros) for continued postdoctoral studies in the group of Dr, 2009.

M. Yao, Visiting Ph.D. student from National University of Singapore) 1 co-­?publication 09, pp.2010-2018, 2013.

. Dr, Loïc Salmon (Ph.D. student) 7 co-­?publications, 2 as co-­?corresponding author 02, pp.2010-2017, 2010.

D. Roldan, Visiting Ph.D. student from Granada, Spain) 3 co-­?publications, 2 as co-­?corresponding author 02, Nikolas Melcher, pp.2007-2014, 2007.

. Bio-­?nmr-annual-user-meeting, C. Brno, and . Republic, Spain (poster) 03/2010 AFMB, Université d'Aix-­?Marseille host: Dr. Sonia Longhi) 01/2010 NMR: A Tool for Biology IX (poster) 01, Conference " Protein Folds in Infectious and Neurodegenerative Diseases EU-­?NMR Annual User Meeting Selskabet for Naturlaerens Udbredelse host: Dr. Leila Lo Leggio) 03 Experimental Nuclear Magnetic Resonance Conference (ENC), Asilomar, California, U.S.A. (poster) 02, pp.5-05, 2006.

. Australian, Murramarang, Australia (poster abstract upgraded to short oral presentation) 05/2005 Symposium of the Danish Instrument Center for NMR Spectroscopy of Biological Macromolecules (poster) 09, New Zealand Magnetic Resonance Conference (ANZMAG) European Experimental Nuclear Magnetic Resonance Conference (EENC), p.6, 2002.

M. R. Jensen, J. L. Ortega-­?roldan, L. Salmon, N. Van-nuland, M. Blackledge et al., In press Characterizing weak protein-­?protein complexes by NMR residual dipolar couplings, Eur. Biophys. J, 2011.

*. Márquez, . J. Embo, F. Leyrat, N. Yabukarski, E. A. Tarbouriech et al., A thermodynamic switch modulates abscisic acid receptor sensitivity Structure of the vesicular stomatitis virus N 0 -­?P complex, Intrinsic disorder in measles virus nucleocapsids " (26) L. Salmon, J.L. Ortega-­?Roldan, E. Lescop, A. Licinio, N. van Nuland, M.R. Jensen*, M, pp.4171-4184, 2011.

*. Blackledge and . Angew, Structure, dynamics, and kinetics of weak protein-­?protein complexes from NMR spin relaxation measurements of titrated solutions " (25), Chem, vol.50, pp.3755-3759, 2011.

*. Longhi, M. R. Leyrat, E. A. Jensen, F. C. Jr, R. W. Gerard et al., Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus The N(0)-­?binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient ?-­?helices, J. Biol. Chem. Blackledge, M. Jamin*. Protein Sci, vol.286, issue.20, pp.13583-13602, 2011.

. Soc, NMR characterization of long-­?range order in intrinsically disordered proteins, pp.8407-8418, 2010.

*. Blackledge, P. Protein, M. R. Letters, *. Jensen, L. Salmon et al., Structural disorder within Sendai virus nucleoprotein and phosphoprotein: Insight into the structural basis of molecular recognition Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts, J. Am. Chem. Soc, vol.17, issue.132, pp.952-960, 2010.

D. F. Gely, C. Lowry, M. R. Bernard, M. Jensen, S. Blackledge et al., Solution structure of the C-­?terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-­?terminal domain of the nucleoprotein Quantitative description of backbone conformational sampling of unfolded proteins at amino acid specific resolution from NMR residual dipolar couplings, J. Mol. Recog. J. Am. Chem. Soc. Structure, vol.23, issue.17, pp.435-447, 2009.

M. Cho, G. Nodet, H. Kim, M. R. Jensen, P. Bernado et al., Structural characterization of ??-synuclein in an aggregation prone state, Protein Science, vol.126, issue.9, pp.1840-1846, 2009.
DOI : 10.1002/pro.194